EP1230333A1 - Process for rinsing fabrics - Google Patents
Process for rinsing fabricsInfo
- Publication number
- EP1230333A1 EP1230333A1 EP00977489A EP00977489A EP1230333A1 EP 1230333 A1 EP1230333 A1 EP 1230333A1 EP 00977489 A EP00977489 A EP 00977489A EP 00977489 A EP00977489 A EP 00977489A EP 1230333 A1 EP1230333 A1 EP 1230333A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- fabric
- reagent
- antibody
- process according
- benefit agent
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Ceased
Links
- 239000004744 fabric Substances 0.000 title claims abstract description 77
- 238000000034 method Methods 0.000 title claims abstract description 41
- 230000008569 process Effects 0.000 title claims abstract description 28
- 230000027455 binding Effects 0.000 claims abstract description 64
- 238000009739 binding Methods 0.000 claims abstract description 63
- 230000008901 benefit Effects 0.000 claims abstract description 43
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 42
- 239000003153 chemical reaction reagent Substances 0.000 claims abstract description 34
- 238000005406 washing Methods 0.000 claims abstract description 11
- 239000000203 mixture Substances 0.000 claims description 30
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 24
- 102000004169 proteins and genes Human genes 0.000 claims description 10
- 108090000623 proteins and genes Proteins 0.000 claims description 10
- 239000000126 substance Substances 0.000 claims description 10
- 229920000742 Cotton Polymers 0.000 claims description 9
- 239000011859 microparticle Substances 0.000 claims description 8
- 239000003205 fragrance Substances 0.000 claims description 7
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 5
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 5
- 239000004902 Softening Agent Substances 0.000 claims description 5
- 239000002304 perfume Substances 0.000 claims description 4
- 239000003223 protective agent Substances 0.000 claims description 4
- 239000007844 bleaching agent Substances 0.000 claims description 3
- 229920000728 polyester Polymers 0.000 claims description 3
- 239000008399 tap water Substances 0.000 description 21
- 235000020679 tap water Nutrition 0.000 description 21
- 239000002245 particle Substances 0.000 description 20
- 150000001875 compounds Chemical class 0.000 description 15
- 239000004094 surface-active agent Substances 0.000 description 15
- 239000003599 detergent Substances 0.000 description 13
- 102000004196 processed proteins & peptides Human genes 0.000 description 13
- 108090000790 Enzymes Proteins 0.000 description 12
- 102000004190 Enzymes Human genes 0.000 description 12
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 12
- 229940088598 enzyme Drugs 0.000 description 12
- 239000000975 dye Substances 0.000 description 11
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
- 239000012634 fragment Substances 0.000 description 9
- -1 aliphatic alcohols Chemical class 0.000 description 8
- 230000000694 effects Effects 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 239000007788 liquid Substances 0.000 description 7
- 239000000427 antigen Substances 0.000 description 6
- 102000036639 antigens Human genes 0.000 description 6
- 108091007433 antigens Proteins 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 229910052708 sodium Inorganic materials 0.000 description 6
- 239000011734 sodium Substances 0.000 description 6
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 5
- 150000001298 alcohols Chemical class 0.000 description 5
- 125000000217 alkyl group Chemical group 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000002736 nonionic surfactant Substances 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 230000009870 specific binding Effects 0.000 description 5
- 102000011022 Chorionic Gonadotropin Human genes 0.000 description 4
- 108010062540 Chorionic Gonadotropin Proteins 0.000 description 4
- 239000003945 anionic surfactant Substances 0.000 description 4
- 238000013459 approach Methods 0.000 description 4
- 102000037865 fusion proteins Human genes 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- 229940084986 human chorionic gonadotropin Drugs 0.000 description 4
- 239000004615 ingredient Substances 0.000 description 4
- 239000003550 marker Substances 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 3
- 241000282832 Camelidae Species 0.000 description 3
- 108010059892 Cellulase Proteins 0.000 description 3
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 3
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 150000001413 amino acids Chemical class 0.000 description 3
- 238000004061 bleaching Methods 0.000 description 3
- 239000003093 cationic surfactant Substances 0.000 description 3
- 229940106157 cellulase Drugs 0.000 description 3
- 238000004140 cleaning Methods 0.000 description 3
- 230000008021 deposition Effects 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 239000007791 liquid phase Substances 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 230000009871 nonspecific binding Effects 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 235000020095 red wine Nutrition 0.000 description 3
- 235000019832 sodium triphosphate Nutrition 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 230000003068 static effect Effects 0.000 description 3
- 239000004753 textile Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 239000004677 Nylon Substances 0.000 description 2
- 108010081873 Persil Proteins 0.000 description 2
- RJKFOVLPORLFTN-LEKSSAKUSA-N Progesterone Chemical compound C1CC2=CC(=O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H](C(=O)C)[C@@]1(C)CC2 RJKFOVLPORLFTN-LEKSSAKUSA-N 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 238000013019 agitation Methods 0.000 description 2
- 229910052783 alkali metal Inorganic materials 0.000 description 2
- 125000000129 anionic group Chemical group 0.000 description 2
- SRSXLGNVWSONIS-UHFFFAOYSA-N benzenesulfonic acid Chemical class OS(=O)(=O)C1=CC=CC=C1 SRSXLGNVWSONIS-UHFFFAOYSA-N 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 235000019864 coconut oil Nutrition 0.000 description 2
- 239000003240 coconut oil Substances 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 239000004816 latex Substances 0.000 description 2
- 229920000126 latex Polymers 0.000 description 2
- 125000005647 linker group Chemical group 0.000 description 2
- 229920001778 nylon Polymers 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 239000003208 petroleum Substances 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- 229910052700 potassium Inorganic materials 0.000 description 2
- 239000011591 potassium Substances 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 230000001235 sensitizing effect Effects 0.000 description 2
- 239000002002 slurry Substances 0.000 description 2
- 150000003384 small molecules Chemical class 0.000 description 2
- 239000002689 soil Substances 0.000 description 2
- 150000003431 steroids Chemical class 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000003760 tallow Substances 0.000 description 2
- XZHKZJXZRWFLCJ-RKFIYKRSSA-N (8R,9S,10S,13R,14S,17R)-17-ethyl-10,13-dimethyl-2,3,4,5,6,7,8,9,11,12,14,17-dodecahydro-1H-cyclopenta[a]phenanthrene-15,16-dione Chemical compound [C@@H]12C(C([C@H](CC)[C@@]1(C)CC[C@H]1[C@H]2CCC2CCCC[C@]12C)=O)=O XZHKZJXZRWFLCJ-RKFIYKRSSA-N 0.000 description 1
- PWCLWZOSAFOXFL-UHPWKVKZSA-N (8s,9s,10r,13s,14s,17s)-17-acetyl-6-hydroxy-10,13-dimethyl-1,2,6,7,8,9,11,12,14,15,16,17-dodecahydrocyclopenta[a]phenanthren-3-one Chemical compound C1C(O)C2=CC(=O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H](C(=O)C)[C@@]1(C)CC2 PWCLWZOSAFOXFL-UHPWKVKZSA-N 0.000 description 1
- AURFZBICLPNKBZ-YZRLXODZSA-N 3alpha-hydroxy-5beta-pregnan-20-one Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H](C(=O)C)[C@@]2(C)CC1 AURFZBICLPNKBZ-YZRLXODZSA-N 0.000 description 1
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 1
- YRNWIFYIFSBPAU-UHFFFAOYSA-N 4-[4-(dimethylamino)phenyl]-n,n-dimethylaniline Chemical compound C1=CC(N(C)C)=CC=C1C1=CC=C(N(C)C)C=C1 YRNWIFYIFSBPAU-UHFFFAOYSA-N 0.000 description 1
- 244000303258 Annona diversifolia Species 0.000 description 1
- 235000002198 Annona diversifolia Nutrition 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000282836 Camelus dromedarius Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 229910002514 Co–Co Inorganic materials 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 1
- OWYWGLHRNBIFJP-UHFFFAOYSA-N Ipazine Chemical compound CCN(CC)C1=NC(Cl)=NC(NC(C)C)=N1 OWYWGLHRNBIFJP-UHFFFAOYSA-N 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- AURFZBICLPNKBZ-UHFFFAOYSA-N Pregnanolone Natural products C1CC2CC(O)CCC2(C)C2C1C1CCC(C(=O)C)C1(C)CC2 AURFZBICLPNKBZ-UHFFFAOYSA-N 0.000 description 1
- GOOHAUXETOMSMM-UHFFFAOYSA-N Propylene oxide Chemical compound CC1CO1 GOOHAUXETOMSMM-UHFFFAOYSA-N 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 229910021536 Zeolite Inorganic materials 0.000 description 1
- FJWGYAHXMCUOOM-QHOUIDNNSA-N [(2s,3r,4s,5r,6r)-2-[(2r,3r,4s,5r,6s)-4,5-dinitrooxy-2-(nitrooxymethyl)-6-[(2r,3r,4s,5r,6s)-4,5,6-trinitrooxy-2-(nitrooxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-3,5-dinitrooxy-6-(nitrooxymethyl)oxan-4-yl] nitrate Chemical compound O([C@@H]1O[C@@H]([C@H]([C@H](O[N+]([O-])=O)[C@H]1O[N+]([O-])=O)O[C@H]1[C@@H]([C@@H](O[N+]([O-])=O)[C@H](O[N+]([O-])=O)[C@@H](CO[N+]([O-])=O)O1)O[N+]([O-])=O)CO[N+](=O)[O-])[C@@H]1[C@@H](CO[N+]([O-])=O)O[C@@H](O[N+]([O-])=O)[C@H](O[N+]([O-])=O)[C@H]1O[N+]([O-])=O FJWGYAHXMCUOOM-QHOUIDNNSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000011149 active material Substances 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 150000004996 alkyl benzenes Chemical class 0.000 description 1
- 125000002947 alkylene group Chemical group 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 239000003429 antifungal agent Substances 0.000 description 1
- 229940121375 antifungal agent Drugs 0.000 description 1
- 239000002216 antistatic agent Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 239000012876 carrier material Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000007859 condensation product Substances 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- HNPSIPDUKPIQMN-UHFFFAOYSA-N dioxosilane;oxo(oxoalumanyloxy)alumane Chemical compound O=[Si]=O.O=[Al]O[Al]=O HNPSIPDUKPIQMN-UHFFFAOYSA-N 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 229950007402 eltanolone Drugs 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 150000002170 ethers Chemical class 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 239000013505 freshwater Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 239000000314 lubricant Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 108010020132 microbial serine proteinases Proteins 0.000 description 1
- 239000003094 microcapsule Substances 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229940079938 nitrocellulose Drugs 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- JZRYQZJSTWVBBD-UHFFFAOYSA-N pentaporphyrin i Chemical class N1C(C=C2NC(=CC3=NC(=C4)C=C3)C=C2)=CC=C1C=C1C=CC4=N1 JZRYQZJSTWVBBD-UHFFFAOYSA-N 0.000 description 1
- 235000020030 perry Nutrition 0.000 description 1
- 230000003711 photoprotective effect Effects 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 150000008442 polyphenolic compounds Chemical class 0.000 description 1
- 235000013824 polyphenols Nutrition 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 150000004032 porphyrins Chemical class 0.000 description 1
- 230000035935 pregnancy Effects 0.000 description 1
- 238000009597 pregnancy test Methods 0.000 description 1
- 150000003138 primary alcohols Chemical class 0.000 description 1
- 239000000186 progesterone Substances 0.000 description 1
- 229960003387 progesterone Drugs 0.000 description 1
- 238000005086 pumping Methods 0.000 description 1
- 125000001453 quaternary ammonium group Chemical group 0.000 description 1
- 230000001846 repelling effect Effects 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 150000003377 silicon compounds Chemical class 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000009987 spinning Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 125000001273 sulfonato group Chemical group [O-]S(*)(=O)=O 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 0.000 description 1
- 230000000475 sunscreen effect Effects 0.000 description 1
- 239000000516 sunscreening agent Substances 0.000 description 1
- 239000000979 synthetic dye Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 239000010457 zeolite Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/0005—Other compounding ingredients characterised by their effect
- C11D3/001—Softening compositions
- C11D3/0015—Softening compositions liquid
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/384—Animal products
- C11D3/3845—Antibodies
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
- C11D2111/10—Objects to be cleaned
- C11D2111/12—Soft surfaces, e.g. textile
Definitions
- the present invention generally relates to a process for rinsing fabrics. More in particular, it relates to a process for rinsing fabrics whereby a benefit agent is delivered to a fabric during the rinse cycle of a washing process.
- a conventional fabric cleaning process as it is carried out in an automated washing machine comprises a main wash cycle (which may comprise a number of sub-cycles) in which soiled fabrics are contacted with a liquid aqueous cleaning composition or wash liquor.
- a main wash cycle which may comprise a number of sub-cycles
- Such a composition comprises surfactants builders and optionally other ingredients such as enzymes, bleaching agents, etc.
- the now cleaned fabrics are subjected to a rinse cycle in which the cleaning composition is removed by pumping it off and spinning the wash load followed by soaking in fresh water.
- softening agents may be added which improve the feel of the washed fabrics .
- Such softening agents conventionally comprise cationic softening compounds of the quaternary ammonium type.
- Other benefit agents include perfumes.
- compositions which are added during the rinse cycle have a relatively short contact time with the fabrics and most of the compounds are immediately removed again in the last centrifuge step.
- O-A-98/00500 discloses a composition comprising a benefit agent attached to a peptide or protein deposition aid which has a high affinity for fabric.
- the composition is claimed to effectively deposit the benefit agent onto the fabric during the wash cycle.
- the transfer of textile dyes from one garment to another during a washing or rinsing process may be inhibited by adding antibodies against the textile dye to the wash or rinse liquid.
- WO-A-98/07820 discloses amongst others rinse treatment compositions containing antibodies directed at cellulase and standard softener actives (such as DEQA) .
- a process for rinsing fabrics whereby a benefit agent is delivered to a fabric during the rinse cycle of a washing process, said benefit agent being deposited onto the fabric by means of a reagent having a high binding affinity for the fabric.
- a rinse composition for use in the process of the invention comprising a reagent having a high binding affinity for the fabric and a benefit agent.
- the invention relates to a process for rinsing fabrics whereby a benefit agent is delivered to a fabric during the rinse cycle of a washing process.
- the benefit agent can be selected from softening agents, finishing agents/ protective agents, fragrances (perfumes), bleaching agents.
- softening agents are clays, cationic surfactants or silicon compounds.
- finishing agents/ protective agents are polymeric lubricants, soil repelling agents, soil release agents, photo-protective agents (sunscreens), anti-static agents, dye-fixing agents, antibacterial agents and anti-fungal agents.
- the fragrances or perfumes may be encapsulated, e.g. in latex microcapsules.
- Suitable examples of bleaches are photobleaches .
- Examples of photobleaches are given in EP-A-379 312 (British Petroleum) , which discloses a water-insoluble photobleach derived from anionically substituted porphine, and in EP-A-035 470 (Ciba Geigy) , which discloses a textile treatment composition comprising a photobleaching component.
- the benefit agent is deposited onto the fabric by means of a reagent having a high binding affinity for the fabric.
- a reagent having a high binding affinity for the fabric.
- a specific example of such a reagent is for instance an antibody.
- the degree of binding of a molecule A to another molecule B can be generally expressed by the chemical equilibrium constant K resulting from the following reaction:
- binding of a molecule to the fabric is specific or not can be judged from the difference between the binding (K d value) of the molecule to one type of fabric, versus the binding to another type of fabric material.
- said material will be a fabric such as cotton or polyester.
- K d value the binding of a molecule to the fabric
- the difference between the two binding constants should be minimally 10, preferably more than 100, and more preferably, more that 1000.
- the reagent should bind to the fabric, with a K d lower than 10 ⁇ 4 M, preferably lower than 10 "6 M and could be 10 ⁇ 10 M or even less.
- K d binding affinities
- the weight efficiency of the reagent in the total rinse composition would be increased and smaller amounts of the reagent would be required.
- Antibodies are specific binding proteins. Their function in nature is to protect against disease by recognising (and binding) foreign bodies, such as viruses or Bacteria, but not self-cells. Furthermore, methods are well-known in the art to generate antibodies that are specific for almost any protein, organic molecule, or cell surface, that is likely to be encountered. This binding specificity has been exploited in the Biotechnology industry, principally for medical diagnostics. For example, many home-based pregnancy test kits comprise an antibody that specifically binds to the pregnancy marker hormone, human chorionic gonadotropin (hCG) , but not to other hormones present in urine.
- hCG human chorionic gonadotropin
- Unilever has described the use of stain-specific antibodies to target bleaching enzymes exclusively to stains but not to dyes - thus achieving efficient stain removal without damaging surrounding fabric.
- Antibodies are well known examples of molecules which are capable of binding specifically to compounds against which they were raised. Antibodies can be derived from several sources. From mice, monoclonal antibodies can be obtained which possess very high binding affinities. From such antibodies, Fab, Fv or scFv fragments, can be prepared which have retained their binding properties. Such antibodies or fragments can be produced through recombinant DNA technology by microbial fermentation. Well known production hosts for antibodies and their fragments are yeast, moulds or bacteria .
- a class of antibodies of particular interest is formed by the Heavy Chain antibodies as found in Camelidae, like the camel or the llama.
- the binding domains of these antibodies consist of a single polypeptide fragment, namely the variable region of the heavy chain polypeptide (HC-V) .
- the binding domain consists of two polypeptide chains (the variable regions of the heavy chain (V h) and the light chain (Vi) ) .
- Procedures to obtain heavy chain immunoglobulins from Camelidae, or ( functionalized) fragments thereof, have been described in WO-A-94/04678 (Casterman and Hamers) and WO-A- 94/25591 (Unilever and Free University of Brussels).
- binding domains can be obtained from the V h fragments of classical antibodies by a procedure termed "camelization" .
- the classical V h fragment is transformed, by substitution of a number of amino acids, into a HC-V-like fragment, whereby its binding properties are retained.
- This procedure has been described by Riechmann et al. in a number of publications (J. Mol . Biol. (1996) 259, 957-969; Protein. Eng . (1996) 9, 531-537, Bio/Technology (1995) 13, 475-479) .
- HC-V fragments can be produced through recombinant DNA technology in a number of microbial hosts (bacterial, yeast, mould), as described in WO-A-94/29457 (Unilever) .
- fusion proteins that comprise an enzyme and an antibody or that comprise an enzyme and an antibody fragment are already known in the art.
- One approach is described by Neuberger and Rabbits (EP-A-194 276) .
- a method for producing a fusion protein comprising an enzyme and an antibody fragment that was derived from an antibody originating in Camelidae is described in WO-A-94/25591.
- a method for producing bispecific antibody fragments is described by Holliger et al. (1993) PNAS 90, 6444-6448.
- a particularly attractive feature of antibody binding behaviour is their reported ability to bind to a "family" of structurally related molecules.
- a "family" of structurally related molecules For example, in Gani et al. (J. Steroid Biochem. Molec. Biol. 48, 277-282) an antibody is described that was raised against progesterone but also binds to the structurally-related steroids, pregnanedione, pregnanolone and 6-hydroxy-progesterone . Therefore, using the same approach, antibodies could be isolated that bind to a whole "family" of stain chromophores (such as the polyphenols, porphyrins, or caretenoids as described below) . A broad action antibody such as this could be used to treat several different stains when coupled to a bleaching enzyme.
- stain chromophores such as the polyphenols, porphyrins, or caretenoids as described below
- Peptides usually have lower binding affinities to the substances of interest than antibodies. Nevertheless, the binding properties of carefully selected or designed peptides can be sufficient to deliver the desired selectivity in an oxidation process.
- a peptide which is capable of binding selectively to a fabric to which one would like to deliver a benefit agent can for instance be obtained from a protein which is known to bind to that specific fabric. An example of such a peptide would be a binding region extracted from an antibody raised against that fabric.
- a suitable peptide could be analogous to the active center of a protein analogous to a non-catalytic binding domain of a protein, e.g. a receptor.
- peptides that bind to such substance can be obtained by the use of peptide combinatorial libraries.
- a library may contain up to 10 10 peptides, from which the peptide with the desired binding properties can be isolated.
- R.A. Houghten Trends in Genetics, Vol 9, no &, 235-239.
- Several embodiments have been described for this procedure (J. Scott et al., Science (1990) 249, 386-390; Fodor et al., Science (1991) 251, 767-773; K. Lam et al., Nature (1991) 354, 82-84; R.A. Houghten et al., Nature (1991) 354, 84-86).
- Suitable peptides can be produced by organic synthesis, using for example the Merrifield procedure (Merrifield (1963) J.Am.Chem.Soc. 85, 2149-2154).
- the peptides can be produced by recombinant DNA technology in microbial hosts (yeast, moulds, bacteria) (K.N. Faber et al. (1996) Appl. Microbiol. Biotechnol . 45, 72-79).
- Pepidomimics In order to improve the stability and/or binding properties of a peptide, the molecule can be modified by the incorporation of non-natural amino acids and/or non-natural chemical linkages between the amino acids. Such molecules are called peptidomimics (H.U. Saragovi et al. (1991) Bio/Technology 10, 773-778; S. Chen et al. (1992)
- the reagent has a high binding affinity for the fabric.
- the reagent is a protein or a peptide, it may be that one part of its polypeptide chain is responsible for the binding affinity to the fabric, and part of the reagent comprises an enzyme part capable of providing a benefit.
- the bleaching enzyme may be a fusion protein comprising two domains, which may be coupled by means of a linker.
- the reagent having the high binding affinity may be covalently coupled to a benefit agent by means of a bivalent coupling agent such as glutardialdehyde.
- a bivalent coupling agent such as glutardialdehyde.
- the reagent having the high binding affinity is a peptide or a protein, it may also be coupled to the enzyme by constructing a fusion protein. In such a construct there would typically be a peptide linker between the binding reagent and the enzyme.
- An example of a fusion of an enzyme and a binding reagent is described in Ducancel et al . Bio/technology 11, 601-605.
- a further embodiment would be for the reagent with a high binding affinity to be a bispecific reagent.
- a reagent could fulfil the requirement of accumulating the benefit agent on the fabric either by supplying said reagent together with the benefit agent as a pre-formed non-covalent complex or by supplying the two separately and allowing them to self-assemble either in the rinse liquor or on the fabric .
- the rinse process of the invention is carried out using micro-particles sensitised with antibody, and configured such that the micro-particles are loaded with the benefit agent and the antibody has a high affinity or specificity for a substance (or "marker molecule" ) typically found on some regions of fabrics but not on others.
- marker molecules include bleach-damaged dyes and microbes known to be associated with malodour.
- the antibody targets the benefit agent to its intended site of action and binds it there.
- Microbe-specific antibodies may target fragrance-containing particles to the regions of malodour. Thus, a more efficient use of expensive ingredients is achieved.
- antibodies specific for bleach-damaged dyes can target dyed particles to faded regions, thus replenishing the colour lost in the main wash cycle.
- micro-particles have been sensitised with antibody and used to generate a coloured end-point in medical diagnostic devices, when they are applied manually onto a test strip.
- analogous particles are being specifically bound to some cotton swatches but not others, depending on which marker molecules are present on the swatches .
- the binding of particles is being driven not by manual application but by agitating a bulk liquid phase (e.g. a rinse liquor) containing said particles and swatches.
- the agitation increases the number of collisions between fabric and particles and thus increases specific binding: particles sensitised with specific antibody result in productive collisions and binding is permanent; particles sensitised with non-specific antibody result in non-productive collisions and do not bind permanently.
- Such an agitation could be readily achieved during the rinse cycle in an automatic washing machine.
- Another advantage of the present invention is that it is possible to target some benefit molecules to particular regions of fabric during the rinse.
- dyes can be targeted to colour-bleached regions to replenish dye lost in the main wash or fragrance can be targeted to regions where it is most needed (i.e. those regions where microbes associated with malodour are present - such as the "underarm" regions).
- methods for targeting small molecules (such as a dye or a fragrance) to particular regions of fabric have not previously been described. The inventors have approached this problem by loading small molecules (such as a dye) onto a micro-particle and then sensitising the particles with an antibody.
- the advantage of this is that a single antibody binding event can deposit many dye molecules onto the target-region of fabric.
- antibody-sensitised particles have been described previously (as component parts of medical diagnostic devices) they are used in a fundamentally different way: in the medical device, the particles are manually applied to the target surface (typically nitro-cellulose paper) and then eluted with a solution. If specific antibody is present, the particles remain stuck on. Otherwise they do not.
- antibody-sensitised particles have not previously been used to target a small chemical compound (such as a dye or a fragrance) from a bulk liquid phase to a particular target site on a surface.
- a small chemical compound such as a dye or a fragrance
- the inventors have been able to achieve surprisingly specific binding to cotton swatches by agitating a bulk liquid phase (of rinse liquor or tap water) containing said particles and swatches.
- An important embodiment of the invention is to use a binding reagent (as described above) that binds to several different types of fabrics. This would have the advantage of enabling a single benefit agent to be deposited to several different types of fabric.
- the rinse compositions of the invention can be used in a detergent composition which is specifically suited for rinsing purposes, and this constitutes a second aspect of the invention.
- WO-A-98/07820 discloses inter alia rinse treatment compositions containing antibodies directed at cellulase and standard softener actives such as DEQA.
- the rinse product according to the present invention preferably contains no softener or low levels of softener active (e.g. HEQ) . If HEQ is present, the rinse product contains Sodium tripolyphosphate (STP) to stabilise antibody activity.
- STP Sodium tripolyphosphate
- the present inventors achieved much superior binding and specificity in rinse liquors (or tap water) by omitting typical softener compositions. They also achieved improved binding in the presence of softener compositions by adding salts, especially multivalent salts such as STP. It is also very surprising that the inventors have found antibodies to be active in rinse liquors (or tap water) . Previously published descriptions of specific antibody binding are typically in physiological strength buffer (0.15M NaCl) often supplemented with 0.15% surfactant. In many ways this mimics the environment in which the antibodies bind in nature, namely in serum which is approximately 0.15M NaCl, pH 7, and where serum albumin may be thought to act in an analogous way to a surfactant in that it reduces the opportunity for non-specific binding reactions .
- the rinse composition comprises one or more benefit agents and optionally other conventional detergent ingredients.
- the invention in its second aspect provides a rinse composition which comprises from 0.1 - 50 % by weight, based on the total composition, of one or more surfactants.
- This surfactant system may in turn comprise 0 - 95 % by weight of one or more anionic surfactants and 5 - 100 % by weight of one or more nonionic surfactants.
- the surfactant system may additionally contain amphoteric or zwitterionic detergent compounds, but this in not normally desired owing to their relatively high cost. It was found to be advantageous to also include cationic surfactants into the composition. Examples of suitable cationic surfactants are given in WO-A-97/03160 and WO-A-98/17767 (Procter&Gamble) .
- nonionic and anionic surfactants of the surfactant system may be chosen from the surfactants described "Surface Active Agents” Vol. 1, by Schwartz & Perry, Interscience 1949, Vol. 2 by Schwartz, Perry & Berch, Interscience 1958, in the current edition of "McCutcheon ' s Emulsifiers and Detergents” published by Manufacturing Confectioners Company or in "Tenside-Taschenbuch” , H. Stache, 2nd Edn., Carl Hauser Verlag, 1981.
- Suitable nonionic detergent compounds which may be used include, in particular, the reaction products of compounds having a hydrophobic group and a reactive hydrogen atom, for example, aliphatic alcohols, acids, amides or alkyl phenols with alkylene oxides, especially ethylene oxide either alone or with propylene oxide.
- Specific nonionic detergent compounds are C 6 -C 22 alkyl phenol-ethylene oxide condensates, generally 5 to 25 EO, i.e. 5 to 25 units of ethylene oxide per molecule, and the condensation products of aliphatic C 8 - Ci 8 primary or secondary linear or branched alcohols with ethylene oxide, generally 5 to 40 EO.
- Suitable anionic detergent compounds which may be used are usually water-soluble alkali metal salts of organic sulphates and sulphonates having alkyl radicals containing from about 8 to about 22 carbon atoms, the term alkyl being used to include the alkyl portion of higher acyl radicals.
- suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulphates, especially those obtained by sulphating higher C 8 -C ⁇ e alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl C 9 -Co benzene sulphonates, particularly sodium linear secondary alkyl C 10 -C 15 benzene sulphonates; and sodium alkyl glyceryl ether sulphates, especially those ethers of the higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum.
- the preferred anionic detergent compounds are sodium Cn-Cis alkyl benzene sulphonates and sodium C ⁇ 2 -C ⁇ e alkyl sulphates.
- surfactants such as those described in EP-A- 328 177 (Unilever), which show resistance to salting-out, the alkyl polyglycoside surfactants described in EP-A-070 074, and alkyl monoglycosides .
- Preferred surfactant systems are mixtures of anionic with nonionic detergent active materials, in particular the groups and examples of anionic and nonionic surfactants pointed out in EP-A-346 995 (Unilever) .
- surfactant system which is a mixture of an alkali metal salt of a C1 6 -C18 primary alcohol sulphate together with a C ⁇ 2 -Ci 5 primary alcohol 3-7 EO ethoxylate.
- the nonionic detergent is preferably present in amounts greater than 10%, e.g. 25-90% by weight of the surfactant system.
- Anionic surfactants can be present for example in amounts in the range from about 5% to about 40% by weight of the surfactant system.
- the rinsing detergent composition may take any suitable physical form, such as a powder, a tablet, an aqueous or non aqueous liquid, a paste or a gel.
- the complex of benefit agent and reagent having a high affinity according to the invention will generally be used as a dilution in water of about 0.05 to 2%.
- the rinse composition in accordance with the invention comprising the complex of the reagent having a high affinity for the fabric and the benefit aid can have any suitable form, i.e. the form of a granular composition, a liquid or a slurry of the enzyme, or with carrier material (e.g. as in EP-A-258 068 and the Savinase (TM) and Lipolase (TM) products of Novo Nordisk) .
- carrier material e.g. as in EP-A-258 068 and the Savinase (TM) and Lipolase (TM) products of Novo Nordisk
- a good way of adding the complex to a liquid rinse product is in the form of a slurry containing from 0.005 to 50 % by weight of the complex in an ethoxylated alcohol nonionic surfactant.
- the rinse compositions of the invention comprise about 0.001 to 10 mg, preferably from 0.01 to 10 mg of antibody per liter of the rinse liquor in use.
- a concentrated rinse composition before use will comprise about 1 to 1000 mg/1, preferably from 10 mg to 100 mg per liter of the rinse product .
- Figure 1 a Graph showing the effects of wash and rinse liquors from Persil non-biological powder main wash on antibody binding activity (a specific anti-hCG monoclonal was used) compared to standard curves in PBST and tap water bench marks) .
- Graph shows binding signal (optical density at 405nm) versus antibody concentration.
- Figure 2 Graph showing the effects of wash and rinse liquors from Zeus liquid main wash on antibody binding activity (a specific anti-hCG monoclonal was used) compared to standard curves in PBST and tap water bench marks .
- Graph shows binding signal (optical density at 405nm) versus antibody concentration.
- Example 1 Antibody binding in Tap water to antigen.
- Antibody activity was determined using an immuno- assay or ⁇ ELISA' .
- the assay comprised a specially designed nylon peg sensitised with antigen.
- a number of wash and rinse liquors were used to determine the effects on antibody activity. These liquors were obtained from wash cycles using standard Persil non-biological powder and Zeus (concentrated zeolite built) non-biological HDL formulation.
- the pegs had to be rehydrated by immersing in phosphate buffer saline (PBS) [0.15M sodium chloride, 0.0075M di-sodium hydrogen ortho- phosphate and 0.0025M sodium di-hydrogen orthophosphate, pH7.2] or distilled water only if using tap water or wash/rinse liquor as antibody diluent, for 15 minutes.
- PBS phosphate buffer saline
- Mouse anti-hCG was assayed as a dilution curve, with concentrations starting at l ⁇ g/ml, in phosphate buffered saline + 0.015% v/v tween 20 (PBST) pH7.2.
- Mouse anti-E3G was assayed as a negative control to allow assessment of non-specific binding and was also run in a dilution curve, with equal concentrations to the mouse anti-hCG.
- the pegs were exposed to the various concentrations of anti-hCG and anti-E3G for 60 minutes, at room temperature, before washing in PBST. This was followed by exposure to Goat anti-mouse alkaline phosphatase conjugate, diluted in PBST, for 30 minutes at room temperature. After a final wash in PBST, the pegs were analysed for the amount of alkaline phosphatase bound by incubating in a colour generating substrate system (p-nitro-phenyl phosphate) where the more antibody bound the more colour is generated. The resulting colour was read in an ELISA plate reader at 405nm.
- Figures 1 and 2 demonstrate the ability of the antibodies to bind to its antigen in tap water and rinse liquors.
- Example 2 Binding antibody loaded particles to fabric senstised with antigen.
- Results The results presented in the table below indicate the ability to target particles to an antigen on fabric via a specific antibody binding event in tap water. The greater the DE the greater the particle deposition. Table 1. Binding of targeted particles to cotton in tap water (non-shaking/static exposure)
- Example 3 Functional bihead antibody molecule in tap water .
- This example describes the confirmation that engineered antibody molecules (with the potential of large-scale exploitation) can function effectively in a non-buffered tap water environment.
- Bi-head molecule (denoted 1349) will bind red wine stains (anti-polyphenolic) and the enzyme Glucose oxidase (Gox) .
- Bi-Head 1349 was diluted at lO ⁇ g/per ml in tap water or Phosphate buffered saline + tween 20, PBST [0.01M Na 2 HPO 4 /NaH 2 PO 4 ,0.15M NaCl and 0.15% Tween 20] each containing 5 ⁇ g/ml Gox. Additionally a control of Gox only at 5 ⁇ g/ml was diluted in tap water or PBST to be used as a control.
- the prepared solutions were dispensed in 1ml volumes to two stained swatches and two unstained swatches. Tap water and PBST only were added to two unstained swatches as a further control. Samples were left at 21°C( ⁇ 1) for 30 minutes without shaking. The samples were placed in bottle containing either tap water or PBST (as appropriate) and agitated on a rototorque (Cole Parmer instrument Co. Chicargo Model 7637-10) for 2 minutes. This rinsing process was repeated twice more. The swatches were then placed in a clean 24 well tissue culture plate and a substrate was added comprising 0.
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Abstract
Description
Claims
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
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EP00977489A EP1230333A1 (en) | 1999-11-16 | 2000-11-03 | Process for rinsing fabrics |
Applications Claiming Priority (4)
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EP99309098 | 1999-11-16 | ||
EP99309098 | 1999-11-16 | ||
PCT/EP2000/010912 WO2001036577A1 (en) | 1999-11-16 | 2000-11-03 | Process for rinsing fabrics |
EP00977489A EP1230333A1 (en) | 1999-11-16 | 2000-11-03 | Process for rinsing fabrics |
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EP1230333A1 true EP1230333A1 (en) | 2002-08-14 |
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EP00977489A Ceased EP1230333A1 (en) | 1999-11-16 | 2000-11-03 | Process for rinsing fabrics |
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EP (1) | EP1230333A1 (en) |
AR (1) | AR026492A1 (en) |
AU (1) | AU1518801A (en) |
BR (1) | BR0015562A (en) |
CA (1) | CA2390076A1 (en) |
WO (1) | WO2001036577A1 (en) |
ZA (1) | ZA200203573B (en) |
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US6946501B2 (en) | 2001-01-31 | 2005-09-20 | The Procter & Gamble Company | Rapidly dissolvable polymer films and articles made therefrom |
US7316994B2 (en) | 2002-11-01 | 2008-01-08 | The Procter & Gamble Company | Perfume polymeric particles |
US8187580B2 (en) | 2002-11-01 | 2012-05-29 | The Procter & Gamble Company | Polymeric assisted delivery using separate addition |
CN105792795B (en) | 2013-11-28 | 2019-09-06 | 荷兰联合利华有限公司 | Improvement relevant to the beneficial agent of encapsulating |
Family Cites Families (5)
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DE19621224A1 (en) * | 1996-05-25 | 1997-11-27 | Henkel Kgaa | Inhibition of dye transfer (colour running) during washing of textiles |
GB9613758D0 (en) * | 1996-07-01 | 1996-09-04 | Unilever Plc | Detergent composition |
AU6953796A (en) * | 1996-08-16 | 1998-03-06 | Procter & Gamble Company, The | Detergent compositions comprising antibody controlled cellulolytic activity |
CA2293304A1 (en) * | 1997-06-13 | 1998-12-17 | Unilever Plc | Bleaching enzymes |
JPH1161639A (en) * | 1997-08-25 | 1999-03-05 | Dainippon Jochugiku Co Ltd | Antimicrobial finishing agent for washing |
-
2000
- 2000-11-03 AU AU15188/01A patent/AU1518801A/en not_active Abandoned
- 2000-11-03 EP EP00977489A patent/EP1230333A1/en not_active Ceased
- 2000-11-03 CA CA002390076A patent/CA2390076A1/en not_active Abandoned
- 2000-11-03 BR BR0015562-4A patent/BR0015562A/en not_active IP Right Cessation
- 2000-11-03 WO PCT/EP2000/010912 patent/WO2001036577A1/en not_active Application Discontinuation
- 2000-11-16 AR ARP000106039A patent/AR026492A1/en not_active Application Discontinuation
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2002
- 2002-05-06 ZA ZA200203573A patent/ZA200203573B/en unknown
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BR0015562A (en) | 2002-09-03 |
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WO2001036577A1 (en) | 2001-05-25 |
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AR026492A1 (en) | 2003-02-12 |
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